Phospholipid dependent mechanism of smp24, an α-helical antimicrobial peptide from scorpion venom

• Published in: Biochimica et biophysica acta Vol. 1858; no. 11; pp. 2737 - 2744
• Main Authors: Harrison, Patrick L., Heath, George R., Johnson, Benjamin R.G., Abdel-Rahman, Mohamed A., Strong, Peter N., Evans, Stephen D., Miller, Keith
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.11.2016
• Subjects: Animals; Antimicrobial Cationic Peptides - chemical synthesis; Antimicrobial Cationic Peptides - pharmacology; Antimicrobial peptides; Atomic force microscopy; Lipid Bilayers - chemistry; Liposomes - chemistry; Membrane damage; Molecular Mimicry; Phosphatidylcholines - chemistry; Phosphatidylethanolamines - chemistry; Phosphatidylglycerols - chemistry; Protein Conformation, alpha-Helical; Quartz crystal microbalance-dissipation; Scorpion Venoms - chemical synthesis; Scorpion Venoms - pharmacology; Scorpions - chemistry; Static Electricity; Atomic force microscopy; Quartz crystal microbalance-dissipation; Membrane damage; Antimicrobial peptides

Determining the mechanism of action of antimicrobial peptides (AMPs) is critical if they are to be developed into the clinical setting. In recent years high resolution techniques such as atomic force microscopy (AFM) have increasingly been utilised to determine AMP mechanism of action on planar lipi...